1OBR
CARBOXYPEPTIDASE T
Experimental procedure
Source type | SYNCHROTRON |
Source details | OTHER |
Temperature [K] | 297 |
Detector technology | FILM |
Collection date | 1987 |
Detector | FILM |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 159.420, 159.420, 106.860 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 7.000 - 2.300 |
Rwork | 0.152 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | CARBOXYPEPTIDASE A (PDB ENTRY 5CPA) |
RMSD bond length | 0.014 |
RMSD bond angle | 0.025 |
Data reduction software | MOSFLM |
Phasing software | BLANC |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
Rmerge | 0.065 |
Number of reflections | 21053 |
Completeness [%] | 61.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | pH 6.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | zinc sulphate | 1 (mM) | |
3 | 1 | drop | MPD | 3 (%) | |
4 | 1 | drop | ammonium sulfate | 35 (%) | |
5 | 1 | drop | MES/NaOH | 50 (mM) |